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bone morphogenetic protein 1; BMP-1; mammalian tolloid protein; mTld; procollagen C-proteinase; PCP (BMP1, PCOLC)

Function: - cleaves the C-terminal propeptides of a) procollagen I b) procollagen II c) procollagen III - induces cartilage & bone formation - may participate in dorsoventral patterning during early development by cleaving chordin (CHRD) - cleavage of the C-terminal propeptide at Ala-|-Asp in procollagen I & procollagens II & at Arg-|-Asp in procollagen III - activity is increased by PCOLCE2 Cofactor: binds 1 Zn+2 per subunit (putative) Structure: - belongs to the peptidase M12A family - contains 5 CUB domains - contains 2 EGF-like domains Alternative splicing: - named isoforms=7 - at least some isoforms may be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay Expression: ubiquitous Comparative biology: - the Drosophila homolog of BMP-1 is the dorsal-ventral patterning protein tolloid

General

bone morphogenetic protein (BMP) zinc metalloprotease

Properties

SIZE: entity length = 986 aa MW = 111 kD COMPARTMENT: extracellular compartment MOTIF: signal sequence {1-22} N-glycosylation site {N91} Metalloprotease {121-321} MOTIF: N-glycosylation site {N142} cysteine residue {C183} MODIFICATION: cysteine residue {C186} cysteine residue {C186} MODIFICATION: cysteine residue {C183} Zn+2-binding site SITE: 213-213 glutamate residue {E214} Zn+2-binding site SITE: 217-217 Zn+2-binding site SITE: 223-223 CUB domain {322-434} MOTIF: cysteine residue {C322} MODIFICATION: cysteine residue {C348} N-glycosylation site {N332} cysteine residue {C348} MODIFICATION: cysteine residue {C322} N-glycosylation site {N363} cysteine residue {C375} MODIFICATION: cysteine residue {C397} cysteine residue {C397} MODIFICATION: cysteine residue {C375} CUB domain {435-546} MOTIF: cysteine residue {C435} MODIFICATION: cysteine residue {C461} cysteine residue {C461} MODIFICATION: cysteine residue {C435} cysteine residue {C488} MODIFICATION: cysteine residue {C510} cysteine residue {C510} MODIFICATION: cysteine residue {C488} EGF domain {547-588} MOTIF: cysteine residue {C551} MODIFICATION: cysteine residue {C563} cysteine residue {C559} MODIFICATION: cysteine residue {C572} cysteine residue {C563} MODIFICATION: cysteine residue {C551} cysteine residue {C572} MODIFICATION: cysteine residue {C559} cysteine residue {C574} MODIFICATION: cysteine residue {C587} cysteine residue {C587} MODIFICATION: cysteine residue {C574} CUB domain {591-703} MOTIF: cysteine residue {C591} MODIFICATION: cysteine residue {C617} N-glycosylation site {N599} cysteine residue {C617} MODIFICATION: cysteine residue {C591} cysteine residue {C644} MODIFICATION: cysteine residue {C666} cysteine residue {C666} MODIFICATION: cysteine residue {C644} EGF domain {704-743} MOTIF: cysteine residue {C707} MODIFICATION: cysteine residue {C718} cysteine residue {C714} MODIFICATION: cysteine residue {C727} cysteine residue {C718} MODIFICATION: cysteine residue {C707} cysteine residue {C727} MODIFICATION: cysteine residue {C714} cysteine residue {C729} MODIFICATION: cysteine residue {C742} cysteine residue {C742} MODIFICATION: cysteine residue {C729} CUB domain {747-859} MOTIF: cysteine residue {C747} MODIFICATION: cysteine residue {C773} cysteine residue {C773} MODIFICATION: cysteine residue {C747} cysteine residue {C800} MODIFICATION: cysteine residue {C822} cysteine residue {C822} MODIFICATION: cysteine residue {C800} CUB domain {860-976} MOTIF: cysteine residue {C860} MODIFICATION: cysteine residue {C890} cysteine residue {C890} MODIFICATION: cysteine residue {C860} cysteine residue {C917} MODIFICATION: cysteine residue {C939} cysteine residue {C939} MODIFICATION: cysteine residue {C917}

Database Correlations

OMIM 112264 UniProt P13497 PFAM correlations Entrez Gene 649 Kegg hsa:649 ENZYME 3.4.24.19

References

  1. UniProt :accession P13497
  2. Entrez Gene :accession 649